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Cryo-EM structure of 8-fold symmetric ratcpn-alpha in apo state

Analyse Cryo-EM structure of 8-fold symmetric ratcpn-alpha in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3J1B
Type: protein
Length: 8,304 residues
Chains: 16
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chaperonin alpha subunit
UniProt: Q877H0
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 49% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Chaperonin alpha subunit	protein	519	49% helix, 17% strand	Q877H0

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	993	0.85	0.86	112	empty
2	867	0.84	0.86	92	empty
3	988	0.84	0.85	107	empty
4	975	0.83	0.85	101	empty
5	1081	0.83	0.84	94	empty

Interfaces

24 interfaces between chains.

N–O · 1252 Å² buried · 13 hydrogen bonds · protein-protein
F–G · 1232 Å² buried · 12 hydrogen bonds · protein-protein
G–H · 1218 Å² buried · 12 hydrogen bonds · protein-protein
D–E · 1208 Å² buried · 10 hydrogen bonds · protein-protein
K–L · 1198 Å² buried · 8 hydrogen bonds · protein-protein

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q877H0
Elsewhere: RCSB PDB 3J1B · PDBe 3J1B · UniProt Q877H0

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